ID SYQ_PSET1 Reviewed; 552 AA. AC Q3IGW8; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 08-NOV-2005, sequence version 1. DT 27-MAR-2024, entry version 118. DE RecName: Full=Glutamine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00126}; DE EC=6.1.1.18 {ECO:0000255|HAMAP-Rule:MF_00126}; DE AltName: Full=Glutaminyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00126}; DE Short=GlnRS {ECO:0000255|HAMAP-Rule:MF_00126}; GN Name=glnS {ECO:0000255|HAMAP-Rule:MF_00126}; GN OrderedLocusNames=PSHAa1642; OS Pseudoalteromonas translucida (strain TAC 125). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales; OC Pseudoalteromonadaceae; Pseudoalteromonas. OX NCBI_TaxID=326442; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TAC 125; RX PubMed=16169927; DOI=10.1101/gr.4126905; RA Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.N., RA Cheung F., Cruveiller S., D'Amico S., Duilio A., Fang G., Feller G., Ho C., RA Mangenot S., Marino G., Nilsson J., Parrilli E., Rocha E.P.C., Rouy Z., RA Sekowska A., Tutino M.L., Vallenet D., von Heijne G., Danchin A.; RT "Coping with cold: the genome of the versatile marine Antarctica bacterium RT Pseudoalteromonas haloplanktis TAC125."; RL Genome Res. 15:1325-1335(2005). CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-glutamine + tRNA(Gln) = AMP + diphosphate + L- CC glutaminyl-tRNA(Gln); Xref=Rhea:RHEA:20121, Rhea:RHEA-COMP:9662, CC Rhea:RHEA-COMP:9681, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, CC ChEBI:CHEBI:58359, ChEBI:CHEBI:78442, ChEBI:CHEBI:78521, CC ChEBI:CHEBI:456215; EC=6.1.1.18; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00126}; CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00126}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00126}. CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family. CC {ECO:0000255|HAMAP-Rule:MF_00126}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CR954246; CAI86715.1; -; Genomic_DNA. DR AlphaFoldDB; Q3IGW8; -. DR SMR; Q3IGW8; -. DR STRING; 326442.PSHAa1642; -. DR KEGG; pha:PSHAa1642; -. DR PATRIC; fig|326442.8.peg.1588; -. DR eggNOG; COG0008; Bacteria. DR HOGENOM; CLU_001882_2_3_6; -. DR BioCyc; PHAL326442:PSHA_RS08050-MONOMER; -. DR Proteomes; UP000006843; Chromosome I. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0004819; F:glutamine-tRNA ligase activity; IEA:UniProtKB-UniRule. DR GO; GO:0006425; P:glutaminyl-tRNA aminoacylation; IEA:InterPro. DR GO; GO:0006424; P:glutamyl-tRNA aminoacylation; IEA:UniProtKB-UniRule. DR CDD; cd00807; GlnRS_core; 1. DR Gene3D; 3.40.50.620; HUPs; 1. DR HAMAP; MF_00126; Gln_tRNA_synth; 1. DR InterPro; IPR001412; aa-tRNA-synth_I_CS. DR InterPro; IPR004514; Gln-tRNA-synth. DR InterPro; IPR022861; Gln_tRNA_ligase_bac. DR InterPro; IPR000924; Glu/Gln-tRNA-synth. DR InterPro; IPR020058; Glu/Gln-tRNA-synth_Ib_cat-dom. DR InterPro; IPR020059; Glu/Gln-tRNA-synth_Ib_codon-bd. DR InterPro; IPR020061; Glu_tRNA_lig_a-bdl. DR InterPro; IPR020056; Rbsml_bL25/Gln-tRNA_synth_N. DR InterPro; IPR011035; Ribosomal_bL25/Gln-tRNA_synth. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR InterPro; IPR049437; tRNA-synt_1c_C2. DR NCBIfam; TIGR00440; glnS; 1. DR PANTHER; PTHR43097:SF4; GLUTAMINE--TRNA LIGASE; 1. DR PANTHER; PTHR43097; GLUTAMINE-TRNA LIGASE; 1. DR Pfam; PF00749; tRNA-synt_1c; 1. DR Pfam; PF03950; tRNA-synt_1c_C; 1. DR Pfam; PF20974; tRNA-synt_1c_C2; 1. DR PRINTS; PR00987; TRNASYNTHGLU. DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1. DR SUPFAM; SSF50715; Ribosomal protein L25-like; 1. DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; KW Nucleotide-binding; Protein biosynthesis; Reference proteome. FT CHAIN 1..552 FT /note="Glutamine--tRNA ligase" FT /id="PRO_1000095501" FT MOTIF 34..44 FT /note="'HIGH' region" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00126" FT MOTIF 268..272 FT /note="'KMSKS' region" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00126" FT BINDING 35..37 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00126" FT BINDING 41..47 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00126" FT BINDING 67 FT /ligand="L-glutamine" FT /ligand_id="ChEBI:CHEBI:58359" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00126" FT BINDING 212 FT /ligand="L-glutamine" FT /ligand_id="ChEBI:CHEBI:58359" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00126" FT BINDING 231 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00126" FT BINDING 261..262 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00126" FT BINDING 269..271 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00126" SQ SEQUENCE 552 AA; 63539 MW; 642BAD8C449B8213 CRC64; MAEIENRPSN FIRTRIDQDL ASGKHASTHT RFPPEPNGFL HIGHAKSICL NFGIAKDYNG LCNLRFDDTN PEKEDINYVN SIKEDVQWLG FNWDGEIKYS SNYFDILYDY AVELINKGLA YVCFLTADQA REYRGTLKEP GKNSPYRDTA SDENLALFEK MRNGEFKEGE CVLRAKIDMA SSFMVLRDPI IYRVRFAHHH QTADKWCIYP MYDFTHCISD ALEGITHSLC TLEFQDNRRL YDWVLDNISL ECHPQQIEFS RLNLEYTIMS KRKLSDLVVN NHVEGWDDPR MPTIAGLRRR GYTPASIREF CLRIGVTKQE NMVEMGMLEA CIREDLNENA PRAMAVLDPV KIVIENYDAD KVETLSVANH PNKEEMGRRD VPFTREIYIE REDFKEEANN KFKRLVLDKE VRLRGAYVIK AQRVEKDENG EITTIYCTYD PETLGKNPSD GRKVKGVIHW VSASEAITAE VRLYDRLFSV PNPAAADEFE STLNPDSLVI LTNAKLEPSL ANSAAEQGFQ FERTGYFSRD SKAKNIVFNQ TVGLRDSWSK TQ //